Research workbench
DNA-binding domain of E2 from human papillomavirus-31, NMR, minimized average structure
Analyse DNA-binding domain of E2 from human papillomavirus-31, NMR, minimized average… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DHM
- Type
- protein
- Length
- 166 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E2 protein
- UniProt
- P17383
Structure
solution nmr · 1 distinct chain · 28% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | E2 protein | protein | 83 | 28% helix, 24% strand | P17383 |
Interfaces
1 interface between chains.
- A–B · 802 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1DHM · DNA-binding domain of E2 from human papillomavirus-31, NMR, minimized average structure · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P17383
- Elsewhere: RCSB PDB 1DHM · PDBe 1DHM · UniProt P17383
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